about
Structure of human procathepsin L reveals the molecular basis of inhibition by the prosegmentSecreted cathepsin L generates endostatin from collagen XVIIIMolecular mechanisms for the conversion of zymogens to active proteolytic enzymesCysteine Proteases: Modes of Activation and Future Prospects as Pharmacological TargetsThe Potential Role of the Proteases Cathepsin D and Cathepsin L in the Progression and Metastasis of Epithelial Ovarian CancerCathepsin B promotes colorectal tumorigenesis, cell invasion, and metastasisAutocatalytic processing of recombinant human procathepsin L. Contribution of both intermolecular and unimolecular events in the processing of procathepsin L in vitroHighly potent inhibitors of human cathepsin L identified by screening combinatorial pentapeptide amide collections.Pericellular mobilization of the tissue-destructive cysteine proteinases, cathepsins B, L, and S, by human monocyte-derived macrophages.Cysteine peptidases of mammals: their biological roles and potential effects in the oral cavity and other tissues in health and disease.Processing and activation of lysosomal proteinases.An Active 32-kDa Cathepsin L Is Secreted Directly from HT 1080 Fibrosarcoma Cells and Not via Lysosomal Exocytosis.The cytoplasmic domain of proEGF negatively regulates motility and elastinolytic activity in thyroid carcinoma cells.CD74: an emerging opportunity as a therapeutic target in cancer and autoimmune disease.Glycosaminoglycans facilitate procathepsin B activation through disruption of propeptide-mature enzyme interactions.Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment.Chondroitin sulfate proteoglycan is a potent enhancer in the processing of procathepsin L.The half-life of human procathepsin S.Multi-step processing of procathepsin L in vitro.Gene regulation and extracellular functions of procathepsin L.Expression and characterization of a recombinant cysteine proteinase of Leishmania mexicana.Cysteine cathepsin activity regulation by glycosaminoglycans.Posttranslational removal of the carboxyl-terminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme.Cell surface-mediated activation of progelatinase A: demonstration of the involvement of the C-terminal domain of progelatinase A in cell surface binding and activation of progelatinase A by primary fibroblasts.Procathepsin L-specific antibodies that recognize procathepsin L but not cathepsin L.Expression and characterization of cathepsin P.Procongopain from Trypanosoma congolense is processed at basic pH: an unusual feature among cathepsin L-like cysteine proteases.Cathepsin L1, the major protease involved in liver fluke (Fasciola hepatica) virulence: propetide cleavage sites and autoactivation of the zymogen secreted from gastrodermal cells.Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.Recombinant human procathepsin S is capable of autocatalytic processing at neutral pH in the presence of glycosaminoglycans.Proteomic analysis of lung metastases in a murine breast cancer model reveals divergent influence of CTSB and CTSL overexpression.Extracellular cathepsin L stimulates axonal growth in neurons.Autocatalytic processing of recombinant human procathepsin B is a bimolecular process.Acidic pH as a physiological regulator of human cathepsin L activity.The major secreted cathepsin L1 protease of the liver fluke, Fasciola hepatica: a Leu-12 to Pro-12 replacement in the nonconserved C-terminal region of the prosegment prevents complete enzyme autoactivation and allows definition of the molecular eveProduction and processing of a recombinant Fasciola hepatica cathepsin B-like enzyme (FhcatB1) reveals potential processing mechanisms in the parasite.
P2860
Q24561952-B8007E0D-620F-4762-A6F6-3207CB65ACDDQ24599981-90513390-AD1A-4568-9F1F-D9F2F1C612DCQ24673104-748F0C3A-DC22-4E2B-BBDA-A5D1669ED140Q26747530-89745580-6D97-4BEA-A5B2-31C873C3A0ADQ26776510-FB4CFC5B-C608-45E5-A40D-5EDC6AE22327Q28259436-3D8205B8-AF7D-4BA9-8841-54F0C829428BQ28262233-8031A119-F3FF-4076-BEBB-0B7890D48A1BQ30897474-1D5C21F3-E406-4999-847E-A554F94D7C74Q34385281-D018F52D-F46F-4C86-89D2-AD219D0D2F06Q34713891-B37CB6E6-45A0-4D58-AA46-40B35CC82CC6Q35055169-FADFC0C9-0733-4A88-BAF8-701E2549B215Q35870565-5C086C05-D6BD-4AAC-A721-D8EFCAE2D1AFQ36897806-E224DA19-9485-4317-A30E-CB0A8D37FB90Q37826194-E13D9CC5-2E0F-43C4-8ED9-4591DE74CDA2Q38298816-53B172E8-11C7-40C6-B5C1-78B98DBF119CQ39406187-7DA9F8E4-6357-4C94-AF86-B7218A33212DQ40674508-C2F5E16F-8B30-444F-B217-F4694398F911Q40932134-462B8722-4BE3-4A5B-9628-6BD0D6FE5DB6Q41436588-7AFF68A1-FA26-4457-85E9-14FBB9060F5AQ41730410-8E7926B2-B1D5-48A0-A17B-FEF7BFB8523AQ41832493-239A77DA-9167-4589-A3F6-C2376FA7569FQ41852264-9521884E-0949-42FD-9DE0-F104CF267BE1Q42058899-15351CDC-3791-4363-B7DB-8D6B898826D0Q42099852-8ECCBF7E-D237-4F10-ADEE-7DE939083560Q42809751-0AEBD2D3-DFA4-4B7D-8315-C53A610E1F8BQ43003548-9F892A73-7B81-427A-8C91-B719E35BC28AQ44529757-579AE191-CB16-49D8-B94D-8C206FA3A32DQ44750364-31CA1541-622E-4260-B2F7-8DB215B6CEF0Q45176585-2E519D52-A704-447D-93DC-57F66DF7665FQ45264641-1B7A6482-1DE4-4EB6-810B-7EB2F93467F4Q46099105-6BCE4FA3-056B-4A22-8160-D3CD0DA0FF12Q47162206-3B8AFC02-431A-4775-BCEB-79E274BAE5A0Q47851086-081AFBD1-C490-46F9-A2EF-08151A96D24BQ52534368-641D6F16-EE21-4974-9B37-212DBF036E79Q53562093-3B67C1ED-FBFE-41C2-A7E6-0544CFB18657Q53606525-9A3A46D5-2BA7-4742-AC07-A4B0F36E8A8E
P2860
description
1992 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1992 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1992
@ast
im Dezember 1992 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 1992/12/30)
@sk
vědecký článek publikovaný v roce 1992
@cs
wetenschappelijk artikel (gepubliceerd op 1992/12/30)
@nl
наукова стаття, опублікована в грудні 1992
@uk
مقالة علمية (نشرت في 30-12-1992)
@ar
name
Surface activation of pro-cathepsin L
@ast
Surface activation of pro-cathepsin L
@en
Surface activation of pro-cathepsin L
@nl
type
label
Surface activation of pro-cathepsin L
@ast
Surface activation of pro-cathepsin L
@en
Surface activation of pro-cathepsin L
@nl
prefLabel
Surface activation of pro-cathepsin L
@ast
Surface activation of pro-cathepsin L
@en
Surface activation of pro-cathepsin L
@nl
P3181
P1476
Surface activation of pro-cathepsin L
@en
P2093
R. W. Mason
S. D. Massey
P304
P3181
P356
10.1016/0006-291X(92)90268-P
P407
P577
1992-12-30T00:00:00Z